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First published online August 20, 2008; 10.1104/pp.108.123117 Plant Physiology 148:1068-1081 (2008) © 2008 American Society of Plant Biologists
slr1923 of Synechocystis sp. PCC6803 Is Essential for Conversion of 3,8-Divinyl(proto)chlorophyll(ide) to 3-Monovinyl(proto)chlorophyll(ide)1Department of Life Science, Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678–1297, Japan (M.R.I., S.A., Y.K., K.S., H.K.); and Department of Life Sciences (Biology), University of Tokyo, Meguro, Tokyo 153–8902, Japan (T.M.)
The deduced amino acid sequence of an slr1923 gene of Synechocystis sp. PCC6803 is homologous to archaean F420H2 dehydrogenase, which acts as a soluble subcomplex of reduced nicotinamide adenine dinucleotide dehydrogenase complex I. In this study, the gene was inactivated and characteristics of the mutant were analyzed. The mutant grew slower than the wild type under 100 µE m–2 s–1 but did not grow under high light intensity (300 µE m–2 s–1). The cellular content of chlorophyll was lower in the mutant, and the absorption spectrum showed a shift in the absorption peak of the Soret band to a longer wavelength by about 10 nm compared with the wild type. It was found, by high-performance liquid chromatography analysis, that the retention time of chlorophyll of the mutant is shorter than that of the wild type and that the peak wavelength of the Soret band was also shifted to a longer wavelength by 11 nm. Proton nuclear magnetic resonance analysis of the chlorophyll of the mutant revealed that the ethyl group of position 8 of ring B is replaced with a vinyl group. The spectrum indicates that the chlorophyll of the mutant is not a normal (3-vinyl)chlorophyll a but a 3,8-divinylchlorophyll a. These results strongly suggest that the Slr1923 protein is essential for the conversion from divinylchlorophyll(ide) to normal chlorophyll(ide). We thus designate this gene cvrA (a gene indispensable for cyanobacterial vinyl reductase).
1 This work was supported by a grant from the 21st Century Center of Excellence Program to K.S. 2 Present address: Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, Kasuga 1-13-27, Bunkyo, Tokyo 112–8551, Japan. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Hiroyuki Koike (hkoike{at}bio.chuo-u.ac.jp). www.plantphysiol.org/cgi/doi/10.1104/pp.108.123117 * Corresponding author; e-mail hkoike{at}bio.chuo-u.ac.jp. Received May 18, 2008; accepted August 14, 2008; published August 20, 2008.
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